HEADER HYDROLASE 18-DEC-08 2W6H
TITLE LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING
TITLE 2 CONTROLLED DEHYDRATION: HYDRATION STATE 4A.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: F1-ATPASE ALPHA SUBUNIT;
COMPND 5 EC: 3.6.3.14;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL;
COMPND 8 CHAIN: D, E, F;
COMPND 9 SYNONYM: F1-ATPASE BETA SUBUNIT;
COMPND 10 EC: 3.6.3.14;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL;
COMPND 13 CHAIN: G;
COMPND 14 SYNONYM: F1-ATPASE GAMMA SUBUNIT;
COMPND 15 EC: 3.6.3.14;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL;
COMPND 18 CHAIN: H;
COMPND 19 SYNONYM: F1-ATPASE DELTA SUBUNIT;
COMPND 20 EC: 3.6.3.14;
COMPND 21 MOL_ID: 5;
COMPND 22 MOLECULE: ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL;
COMPND 23 CHAIN: I;
COMPND 24 SYNONYM: F1-ATPASE EPSILON SUBUNIT;
COMPND 25 EC: 3.6.3.14
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: HEART;
SOURCE 6 TISSUE: MUSCLE;
SOURCE 7 ORGANELLE: MITOCHONDRIA;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 10 ORGANISM_COMMON: BOVINE;
SOURCE 11 ORGANISM_TAXID: 9913;
SOURCE 12 ORGAN: HEART;
SOURCE 13 TISSUE: MUSCLE;
SOURCE 14 ORGANELLE: MITOCHONRIA;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 17 ORGANISM_COMMON: BOVINE;
SOURCE 18 ORGANISM_TAXID: 9913;
SOURCE 19 ORGAN: HEART;
SOURCE 20 TISSUE: MUSCLE;
SOURCE 21 ORGANELLE: MITOCHONRIA;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 24 ORGANISM_COMMON: BOVINE;
SOURCE 25 ORGANISM_TAXID: 9913;
SOURCE 26 ORGAN: HEART;
SOURCE 27 TISSUE: MUSCLE;
SOURCE 28 ORGANELLE: MITOCHONRIA;
SOURCE 29 MOL_ID: 5;
SOURCE 30 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 31 ORGANISM_COMMON: BOVINE;
SOURCE 32 ORGANISM_TAXID: 9913;
SOURCE 33 ORGAN: HEART;
SOURCE 34 TISSUE: MUSCLE;
SOURCE 35 ORGANELLE: MITOCHONRIA
KEYWDS ATP PHOSPHORYLASE (H+ TRANSPORTING), TRANSIT PEPTIDE, F1FO ATP
KEYWDS 2 SYNTHASE, ATP PHOSPHORYLASE, ATP SYNTHASE, ION TRANSPORT,
KEYWDS 3 MITOCHONDRION, ATP SYNTHESIS, UBL CONJUGATION, CF(1), P-LOOP,
KEYWDS 4 HYDROLASE, NUCLEOTIDE-BINDING, HYDROGEN ION TRANSPORT, PYRROLIDONE
KEYWDS 5 CARBOXYLIC ACID, ATP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SANCHEZ-WEATHERBY,F.FELISAZ,A.GOBBO,J.HUET,R.B.G.RAVELLI,
AUTHOR 2 M.W.BOWLER,F.CIPRIANI
REVDAT 5 13-DEC-23 2W6H 1 REMARK
REVDAT 4 16-JAN-19 2W6H 1 JRNL
REVDAT 3 16-JUN-10 2W6H 1 KEYWDS JRNL REMARK
REVDAT 2 24-NOV-09 2W6H 1 JRNL
REVDAT 1 27-OCT-09 2W6H 0
JRNL AUTH J.SANCHEZ-WEATHERBY,M.W.BOWLER,J.HUET,A.GOBBO,F.FELISAZ,
JRNL AUTH 2 B.LAVAULT,R.MOYA,J.KADLEC,R.B.RAVELLI,F.CIPRIANI
JRNL TITL IMPROVING DIFFRACTION BY HUMIDITY CONTROL: A NOVEL DEVICE
JRNL TITL 2 COMPATIBLE WITH X-RAY BEAMLINES.
JRNL REF ACTA CRYSTALLOGR. D BIOL. V. 65 1237 2009
JRNL REF 2 CRYSTALLOGR.
JRNL REFN ESSN 1399-0047
JRNL PMID 19966409
JRNL DOI 10.1107/S0907444909037822
REMARK 2
REMARK 2 RESOLUTION. 5.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0038
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 5.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 18266
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.296
REMARK 3 R VALUE (WORKING SET) : 0.296
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 5.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 5.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1303
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : 0.0000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 25108
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.25000
REMARK 3 B22 (A**2) : -1.90000
REMARK 3 B33 (A**2) : 2.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.734
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.000
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.005
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.807
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. THE DATA WERE COLLECTED AT ROOM TEMPERATURE, DURING
REMARK 3 CONTROLLED DEHYDRATION OF CRYSTALS,TO EVALUATE THE CHANGES THAT
REMARK 3 OCCUR IN CRYSTAL PACKING DURING DEHYDRATION. NO BIOLOGICAL
REMARK 3 SIGNIFICANCE SHOULD BE ATTACHED TO THE COORDINATES.
REMARK 4
REMARK 4 2W6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1290038380.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 294
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : DIAMOND111
REMARK 200 OPTICS : GE211
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18314
REMARK 200 RESOLUTION RANGE HIGH (A) : 5.000
REMARK 200 RESOLUTION RANGE LOW (A) : 62.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.20000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 5.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1BMF
REMARK 200
REMARK 200 REMARK: THE DATA WERE COLLECTED AT ROOM TEMPERATURE, DURING
REMARK 200 CONTROLLED DEHYDRATION OF CRYSTALS,TO EVALUATE THE CHANGES THAT
REMARK 200 OCCUR IN CRYSTAL PACKING DURING DEHYDRATION. NO BIOLOGICAL
REMARK 200 SIGNIFICANCE SHOULD BE ATTACHED TO THE COORDINATES.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS-HCL PH 8.2, 200 MM NACL, 20
REMARK 280 MM MGSO4, 1 MM ADP, 1 MM ALCL3, 6 MM NAF 0.004% (W/V)
REMARK 280 PHENYLMETHYLSULFONYL FLUORIDE AND 12% (W/V) POLYETHYLENE GLYCOL
REMARK 280 6000, PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 53.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 134.33000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.12000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 134.33000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.12000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: NONAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 43360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 143010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -220.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -42
REMARK 465 LEU A -41
REMARK 465 SER A -40
REMARK 465 VAL A -39
REMARK 465 ARG A -38
REMARK 465 VAL A -37
REMARK 465 ALA A -36
REMARK 465 ALA A -35
REMARK 465 ALA A -34
REMARK 465 VAL A -33
REMARK 465 ALA A -32
REMARK 465 ARG A -31
REMARK 465 ALA A -30
REMARK 465 LEU A -29
REMARK 465 PRO A -28
REMARK 465 ARG A -27
REMARK 465 ARG A -26
REMARK 465 ALA A -25
REMARK 465 GLY A -24
REMARK 465 LEU A -23
REMARK 465 VAL A -22
REMARK 465 SER A -21
REMARK 465 LYS A -20
REMARK 465 ASN A -19
REMARK 465 ALA A -18
REMARK 465 LEU A -17
REMARK 465 GLY A -16
REMARK 465 SER A -15
REMARK 465 SER A -14
REMARK 465 PHE A -13
REMARK 465 ILE A -12
REMARK 465 ALA A -11
REMARK 465 ALA A -10
REMARK 465 ARG A -9
REMARK 465 ASN A -8
REMARK 465 LEU A -7
REMARK 465 HIS A -6
REMARK 465 ALA A -5
REMARK 465 SER A -4
REMARK 465 ASN A -3
REMARK 465 SER A -2
REMARK 465 ARG A -1
REMARK 465 LEU A 0
REMARK 465 GLN A 1
REMARK 465 LYS A 2
REMARK 465 THR A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 8
REMARK 465 SER A 9
REMARK 465 SER A 10
REMARK 465 ILE A 11
REMARK 465 LEU A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 ARG A 15
REMARK 465 ILE A 16
REMARK 465 LEU A 17
REMARK 465 GLY A 18
REMARK 465 ALA A 19
REMARK 465 ASP A 20
REMARK 465 THR A 21
REMARK 465 SER A 22
REMARK 465 VAL A 23
REMARK 465 MET B -42
REMARK 465 LEU B -41
REMARK 465 SER B -40
REMARK 465 VAL B -39
REMARK 465 ARG B -38
REMARK 465 VAL B -37
REMARK 465 ALA B -36
REMARK 465 ALA B -35
REMARK 465 ALA B -34
REMARK 465 VAL B -33
REMARK 465 ALA B -32
REMARK 465 ARG B -31
REMARK 465 ALA B -30
REMARK 465 LEU B -29
REMARK 465 PRO B -28
REMARK 465 ARG B -27
REMARK 465 ARG B -26
REMARK 465 ALA B -25
REMARK 465 GLY B -24
REMARK 465 LEU B -23
REMARK 465 VAL B -22
REMARK 465 SER B -21
REMARK 465 LYS B -20
REMARK 465 ASN B -19
REMARK 465 ALA B -18
REMARK 465 LEU B -17
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 SER B -14
REMARK 465 PHE B -13
REMARK 465 ILE B -12
REMARK 465 ALA B -11
REMARK 465 ALA B -10
REMARK 465 ARG B -9
REMARK 465 ASN B -8
REMARK 465 LEU B -7
REMARK 465 HIS B -6
REMARK 465 ALA B -5
REMARK 465 SER B -4
REMARK 465 ASN B -3
REMARK 465 SER B -2
REMARK 465 ARG B -1
REMARK 465 LEU B 0
REMARK 465 GLN B 1
REMARK 465 LYS B 2
REMARK 465 THR B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 ALA B 6
REMARK 465 GLU B 7
REMARK 465 VAL B 8
REMARK 465 SER B 9
REMARK 465 SER B 10
REMARK 465 ILE B 11
REMARK 465 LEU B 12
REMARK 465 GLU B 13
REMARK 465 GLU B 14
REMARK 465 ARG B 15
REMARK 465 ILE B 16
REMARK 465 LEU B 17
REMARK 465 GLY B 18
REMARK 465 ALA B 19
REMARK 465 ASP B 20
REMARK 465 THR B 21
REMARK 465 SER B 22
REMARK 465 VAL B 23
REMARK 465 ALA B 402
REMARK 465 PHE B 403
REMARK 465 ALA B 404
REMARK 465 GLN B 405
REMARK 465 PHE B 406
REMARK 465 GLY B 407
REMARK 465 SER B 408
REMARK 465 ASP B 409
REMARK 465 MET C -42
REMARK 465 LEU C -41
REMARK 465 SER C -40
REMARK 465 VAL C -39
REMARK 465 ARG C -38
REMARK 465 VAL C -37
REMARK 465 ALA C -36
REMARK 465 ALA C -35
REMARK 465 ALA C -34
REMARK 465 VAL C -33
REMARK 465 ALA C -32
REMARK 465 ARG C -31
REMARK 465 ALA C -30
REMARK 465 LEU C -29
REMARK 465 PRO C -28
REMARK 465 ARG C -27
REMARK 465 ARG C -26
REMARK 465 ALA C -25
REMARK 465 GLY C -24
REMARK 465 LEU C -23
REMARK 465 VAL C -22
REMARK 465 SER C -21
REMARK 465 LYS C -20
REMARK 465 ASN C -19
REMARK 465 ALA C -18
REMARK 465 LEU C -17
REMARK 465 GLY C -16
REMARK 465 SER C -15
REMARK 465 SER C -14
REMARK 465 PHE C -13
REMARK 465 ILE C -12
REMARK 465 ALA C -11
REMARK 465 ALA C -10
REMARK 465 ARG C -9
REMARK 465 ASN C -8
REMARK 465 LEU C -7
REMARK 465 HIS C -6
REMARK 465 ALA C -5
REMARK 465 SER C -4
REMARK 465 ASN C -3
REMARK 465 SER C -2
REMARK 465 ARG C -1
REMARK 465 LEU C 0
REMARK 465 GLN C 1
REMARK 465 LYS C 2
REMARK 465 THR C 3
REMARK 465 GLY C 4
REMARK 465 THR C 5
REMARK 465 ALA C 6
REMARK 465 GLU C 7
REMARK 465 VAL C 8
REMARK 465 SER C 9
REMARK 465 SER C 10
REMARK 465 ILE C 11
REMARK 465 LEU C 12
REMARK 465 GLU C 13
REMARK 465 GLU C 14
REMARK 465 ARG C 15
REMARK 465 ILE C 16
REMARK 465 LEU C 17
REMARK 465 GLY C 18
REMARK 465 MET D -49
REMARK 465 LEU D -48
REMARK 465 GLY D -47
REMARK 465 LEU D -46
REMARK 465 VAL D -45
REMARK 465 GLY D -44
REMARK 465 ARG D -43
REMARK 465 VAL D -42
REMARK 465 VAL D -41
REMARK 465 ALA D -40
REMARK 465 ALA D -39
REMARK 465 SER D -38
REMARK 465 ALA D -37
REMARK 465 SER D -36
REMARK 465 GLY D -35
REMARK 465 ALA D -34
REMARK 465 LEU D -33
REMARK 465 ARG D -32
REMARK 465 GLY D -31
REMARK 465 LEU D -30
REMARK 465 SER D -29
REMARK 465 PRO D -28
REMARK 465 SER D -27
REMARK 465 ALA D -26
REMARK 465 PRO D -25
REMARK 465 LEU D -24
REMARK 465 PRO D -23
REMARK 465 GLN D -22
REMARK 465 ALA D -21
REMARK 465 GLN D -20
REMARK 465 LEU D -19
REMARK 465 LEU D -18
REMARK 465 LEU D -17
REMARK 465 ARG D -16
REMARK 465 ALA D -15
REMARK 465 ALA D -14
REMARK 465 PRO D -13
REMARK 465 ALA D -12
REMARK 465 ALA D -11
REMARK 465 LEU D -10
REMARK 465 GLN D -9
REMARK 465 PRO D -8
REMARK 465 ALA D -7
REMARK 465 ARG D -6
REMARK 465 ASP D -5
REMARK 465 TYR D -4
REMARK 465 ALA D -3
REMARK 465 ALA D -2
REMARK 465 GLN D -1
REMARK 465 ALA D 0
REMARK 465 SER D 1
REMARK 465 PRO D 2
REMARK 465 SER D 3
REMARK 465 PRO D 4
REMARK 465 LYS D 5
REMARK 465 ALA D 6
REMARK 465 GLY D 7
REMARK 465 ALA D 8
REMARK 465 GLU D 476
REMARK 465 HIS D 477
REMARK 465 SER D 478
REMARK 465 MET E -49
REMARK 465 LEU E -48
REMARK 465 GLY E -47
REMARK 465 LEU E -46
REMARK 465 VAL E -45
REMARK 465 GLY E -44
REMARK 465 ARG E -43
REMARK 465 VAL E -42
REMARK 465 VAL E -41
REMARK 465 ALA E -40
REMARK 465 ALA E -39
REMARK 465 SER E -38
REMARK 465 ALA E -37
REMARK 465 SER E -36
REMARK 465 GLY E -35
REMARK 465 ALA E -34
REMARK 465 LEU E -33
REMARK 465 ARG E -32
REMARK 465 GLY E -31
REMARK 465 LEU E -30
REMARK 465 SER E -29
REMARK 465 PRO E -28
REMARK 465 SER E -27
REMARK 465 ALA E -26
REMARK 465 PRO E -25
REMARK 465 LEU E -24
REMARK 465 PRO E -23
REMARK 465 GLN E -22
REMARK 465 ALA E -21
REMARK 465 GLN E -20
REMARK 465 LEU E -19
REMARK 465 LEU E -18
REMARK 465 LEU E -17
REMARK 465 ARG E -16
REMARK 465 ALA E -15
REMARK 465 ALA E -14
REMARK 465 PRO E -13
REMARK 465 ALA E -12
REMARK 465 ALA E -11
REMARK 465 LEU E -10
REMARK 465 GLN E -9
REMARK 465 PRO E -8
REMARK 465 ALA E -7
REMARK 465 ARG E -6
REMARK 465 ASP E -5
REMARK 465 TYR E -4
REMARK 465 ALA E -3
REMARK 465 ALA E -2
REMARK 465 GLN E -1
REMARK 465 ALA E 0
REMARK 465 SER E 1
REMARK 465 PRO E 2
REMARK 465 SER E 3
REMARK 465 PRO E 4
REMARK 465 LYS E 5
REMARK 465 ALA E 6
REMARK 465 GLY E 7
REMARK 465 ALA E 8
REMARK 465 GLU E 475
REMARK 465 GLU E 476
REMARK 465 HIS E 477
REMARK 465 SER E 478
REMARK 465 MET F -49
REMARK 465 LEU F -48
REMARK 465 GLY F -47
REMARK 465 LEU F -46
REMARK 465 VAL F -45
REMARK 465 GLY F -44
REMARK 465 ARG F -43
REMARK 465 VAL F -42
REMARK 465 VAL F -41
REMARK 465 ALA F -40
REMARK 465 ALA F -39
REMARK 465 SER F -38
REMARK 465 ALA F -37
REMARK 465 SER F -36
REMARK 465 GLY F -35
REMARK 465 ALA F -34
REMARK 465 LEU F -33
REMARK 465 ARG F -32
REMARK 465 GLY F -31
REMARK 465 LEU F -30
REMARK 465 SER F -29
REMARK 465 PRO F -28
REMARK 465 SER F -27
REMARK 465 ALA F -26
REMARK 465 PRO F -25
REMARK 465 LEU F -24
REMARK 465 PRO F -23
REMARK 465 GLN F -22
REMARK 465 ALA F -21
REMARK 465 GLN F -20
REMARK 465 LEU F -19
REMARK 465 LEU F -18
REMARK 465 LEU F -17
REMARK 465 ARG F -16
REMARK 465 ALA F -15
REMARK 465 ALA F -14
REMARK 465 PRO F -13
REMARK 465 ALA F -12
REMARK 465 ALA F -11
REMARK 465 LEU F -10
REMARK 465 GLN F -9
REMARK 465 PRO F -8
REMARK 465 ALA F -7
REMARK 465 ARG F -6
REMARK 465 ASP F -5
REMARK 465 TYR F -4
REMARK 465 ALA F -3
REMARK 465 ALA F -2
REMARK 465 GLN F -1
REMARK 465 ALA F 0
REMARK 465 SER F 1
REMARK 465 PRO F 2
REMARK 465 SER F 3
REMARK 465 PRO F 4
REMARK 465 LYS F 5
REMARK 465 ALA F 6
REMARK 465 GLY F 7
REMARK 465 ALA F 8
REMARK 465 GLU F 475
REMARK 465 GLU F 476
REMARK 465 HIS F 477
REMARK 465 SER F 478
REMARK 465 MET G -24
REMARK 465 PHE G -23
REMARK 465 SER G -22
REMARK 465 ARG G -21
REMARK 465 ALA G -20
REMARK 465 GLY G -19
REMARK 465 VAL G -18
REMARK 465 ALA G -17
REMARK 465 GLY G -16
REMARK 465 LEU G -15
REMARK 465 SER G -14
REMARK 465 ALA G -13
REMARK 465 TRP G -12
REMARK 465 THR G -11
REMARK 465 VAL G -10
REMARK 465 GLN G -9
REMARK 465 PRO G -8
REMARK 465 GLN G -7
REMARK 465 TRP G -6
REMARK 465 ILE G -5
REMARK 465 GLN G -4
REMARK 465 VAL G -3
REMARK 465 ARG G -2
REMARK 465 ASN G -1
REMARK 465 MET G 0
REMARK 465 ASP G 62
REMARK 465 LYS G 63
REMARK 465 LYS G 64
REMARK 465 LYS G 65
REMARK 465 HIS G 66
REMARK 465 ALA G 97
REMARK 465 ALA G 98
REMARK 465 ALA G 99
REMARK 465 GLY G 100
REMARK 465 ASP G 273
REMARK 465 MET H -21
REMARK 465 LEU H -20
REMARK 465 PRO H -19
REMARK 465 SER H -18
REMARK 465 ALA H -17
REMARK 465 LEU H -16
REMARK 465 LEU H -15
REMARK 465 ARG H -14
REMARK 465 ARG H -13
REMARK 465 PRO H -12
REMARK 465 GLY H -11
REMARK 465 LEU H -10
REMARK 465 GLY H -9
REMARK 465 ARG H -8
REMARK 465 LEU H -7
REMARK 465 VAL H -6
REMARK 465 ARG H -5
REMARK 465 GLN H -4
REMARK 465 VAL H -3
REMARK 465 ARG H -2
REMARK 465 LEU H -1
REMARK 465 TYR H 0
REMARK 465 ALA H 1
REMARK 465 GLU H 2
REMARK 465 ALA H 3
REMARK 465 ALA H 4
REMARK 465 ALA H 5
REMARK 465 ALA H 6
REMARK 465 GLN H 7
REMARK 465 ALA H 8
REMARK 465 PRO H 9
REMARK 465 ALA H 10
REMARK 465 ALA H 11
REMARK 465 GLY H 12
REMARK 465 PRO H 13
REMARK 465 GLY H 14
REMARK 465 GLU H 146
REMARK 465 MET I 0
REMARK 465 LYS I 48
REMARK 465 LYS I 49
REMARK 465 GLU I 50
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 481 CB OG
REMARK 470 SER B 481 CB OG
REMARK 470 SER C 481 CB OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE ARG B 45 CZ ARG H 128 2554 1.86
REMARK 500 CD ARG B 45 NH2 ARG H 128 2554 2.04
REMARK 500 NE ARG B 45 NH1 ARG H 128 2554 2.15
REMARK 500 NE ARG B 45 NH2 ARG H 128 2554 2.15
REMARK 500 OE2 GLU B 26 O ALA H 122 2554 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 106 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 170 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 171 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 210 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 270 CB - CA - C ANGL. DEV. = -14.2 DEGREES
REMARK 500 VAL A 371 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 SER A 372 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 373 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 398 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 398 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 420 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 450 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 450 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 40 CD - NE - CZ ANGL. DEV. = 13.8 DEGREES
REMARK 500 ARG B 40 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG B 127 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG B 128 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 219 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 219 NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG B 258 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ASP B 270 CB - CA - C ANGL. DEV. = -14.8 DEGREES
REMARK 500 ASP B 270 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 279 CD - NE - CZ ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG B 279 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG B 279 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TYR B 300 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 304 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG B 304 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 GLN B 349 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 VAL B 371 CB - CA - C ANGL. DEV. = -11.7 DEGREES
REMARK 500 ARG B 423 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG C 45 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG C 127 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG C 161 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG C 161 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG C 164 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG C 258 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG C 291 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 291 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG C 304 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG C 308 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 308 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 362 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG C 381 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG C 423 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG C 450 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG C 450 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 HIS C 476 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 ARG D 44 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 89 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 57 -17.49 -39.81
REMARK 500 PRO A 138 4.96 -65.96
REMARK 500 VAL A 157 51.97 -144.82
REMARK 500 ALA A 246 -55.62 -22.25
REMARK 500 ASN A 260 41.38 -94.45
REMARK 500 ALA A 364 28.79 -65.68
REMARK 500 ALA A 377 -8.79 -52.53
REMARK 500 ALA A 401 -57.39 -27.17
REMARK 500 ALA A 404 -73.67 -25.89
REMARK 500 GLN A 405 2.00 -53.54
REMARK 500 SER A 408 -9.30 -58.96
REMARK 500 ASP A 409 59.50 178.50
REMARK 500 TYR A 433 17.35 56.55
REMARK 500 HIS A 476 40.51 -101.56
REMARK 500 GLN A 477 0.54 -68.08
REMARK 500 ARG A 484 -74.82 -54.06
REMARK 500 THR A 485 -70.80 -47.51
REMARK 500 GLU A 492 -73.39 -69.13
REMARK 500 GLU A 509 41.60 -103.30
REMARK 500 SER B 33 135.83 -171.68
REMARK 500 SER B 56 -37.42 -39.23
REMARK 500 LEU B 64 -60.37 -92.01
REMARK 500 PRO B 68 -14.70 -45.10
REMARK 500 ASP B 69 34.26 -157.79
REMARK 500 ASN B 70 162.41 173.34
REMARK 500 THR B 91 -2.57 -145.02
REMARK 500 VAL B 95 125.72 -34.66
REMARK 500 LYS B 118 35.00 -94.38
REMARK 500 GLN B 208 -179.50 -68.23
REMARK 500 ALA B 246 -56.65 -27.09
REMARK 500 ASN B 260 54.91 -112.34
REMARK 500 LYS B 359 -2.32 -55.09
REMARK 500 ALA B 364 40.22 -64.04
REMARK 500 GLU B 399 -71.33 -58.90
REMARK 500 ASP B 411 118.76 67.75
REMARK 500 ALA B 413 -72.45 -56.28
REMARK 500 TYR B 452 5.00 -57.42
REMARK 500 PRO B 458 -33.99 -32.77
REMARK 500 HIS B 476 52.40 -112.12
REMARK 500 VAL C 23 54.71 -117.40
REMARK 500 ASP C 79 3.30 -69.30
REMARK 500 ASP C 86 151.60 -45.82
REMARK 500 PRO C 138 1.83 -69.64
REMARK 500 GLN C 208 -179.02 -62.92
REMARK 500 ALA C 246 -54.45 -28.72
REMARK 500 GLU C 292 16.47 53.57
REMARK 500 ALA C 293 -13.60 88.00
REMARK 500 ALA C 336 138.67 -37.62
REMARK 500 ASP C 347 38.85 -93.13
REMARK 500 ALA C 364 38.19 -79.99
REMARK 500
REMARK 500 THIS ENTRY HAS 150 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 13-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 14-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JIZ RELATED DB: PDB
REMARK 900 THE STRUCTURES OF F1-ATPASE INHIBITED BY RESVERATROL, PICEATANNOL
REMARK 900 AND QUERCETIN.
REMARK 900 RELATED ID: 2V7Q RELATED DB: PDB
REMARK 900 THE STRUCTURE OF F1-ATPASE INHIBITED BY I1 -60HIS, A MONOMERIC FORM
REMARK 900 OF THE INHIBITOR PROTEIN, IF1.
REMARK 900 RELATED ID: 1NBM RELATED DB: PDB
REMARK 900 THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-
REMARK 900 CHLORO-7-NITROBENZOFURAZAN
REMARK 900 RELATED ID: 1BMF RELATED DB: PDB
REMARK 900 BOVINE MITOCHONDRIAL F1-ATPASE
REMARK 900 RELATED ID: 2JJ1 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF F1-ATPASE INHIBITED BY PICEATANNOL.
REMARK 900 RELATED ID: 1E1Q RELATED DB: PDB
REMARK 900 BOVINE MITOCHONDRIAL F1-ATPASE AT 100K
REMARK 900 RELATED ID: 1W0J RELATED DB: PDB
REMARK 900 BERYLLIUM FLUORIDE INHIBITED BOVINE F1-ATPASE
REMARK 900 RELATED ID: 1COW RELATED DB: PDB
REMARK 900 BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH AUROVERTIN B
REMARK 900 RELATED ID: 1H8H RELATED DB: PDB
REMARK 900 BOVINE MITOCHONDRIAL F1-ATPASE AT 100K
REMARK 900 RELATED ID: 1E1R RELATED DB: PDB
REMARK 900 BOVINE MITOCHONDRIAL F1-ATPASE INHIBITED BY MG2+ADP AND ALUMINIUM
REMARK 900 FLUORIDE
REMARK 900 RELATED ID: 1OHH RELATED DB: PDB
REMARK 900 BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE INHIBITOR PROTEIN
REMARK 900 IF1
REMARK 900 RELATED ID: 1QO1 RELATED DB: PDB
REMARK 900 MOLECULAR ARCHITECTURE OF THE ROTARY MOTOR IN ATP SYNTHASE FROM
REMARK 900 YEASTMITOCHONDRIA
REMARK 900 RELATED ID: 2JDI RELATED DB: PDB
REMARK 900 GROUND STATE STRUCTURE OF F1-ATPASE FROM BOVINE HEART MITOCHONDRIA
REMARK 900 (BOVINE F1-ATPASE CRYSTALLISED IN THE ABSENCE OF AZIDE)
REMARK 900 RELATED ID: 1H8E RELATED DB: PDB
REMARK 900 (ADP.ALF4)2(ADP.SO4) BOVINE F1-ATPASE ( ALL THREE CATALYTIC SITES
REMARK 900 OCCUPIED)
REMARK 900 RELATED ID: 1EFR RELATED DB: PDB
REMARK 900 BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE
REMARK 900 ANTIBIOTIC EFRAPEPTIN
REMARK 900 RELATED ID: 2JJ2 RELATED DB: PDB
REMARK 900 THE STRUCTURES OF F1-ATPASE INHIBITED BY QUERCETIN.
REMARK 900 RELATED ID: 1E79 RELATED DB: PDB
REMARK 900 BOVINE F1-ATPASE INHIBITED BY DCCD( DICYCLOHEXYLCARBODIIMIDE)
REMARK 900 RELATED ID: 2CK3 RELATED DB: PDB
REMARK 900 AZIDE INHIBITED BOVINE F1-ATPASE
REMARK 900 RELATED ID: 1W0K RELATED DB: PDB
REMARK 900 BERYLLIUM FLUORIDE INHIBITED BOVINE F1-ATPASE
REMARK 900 RELATED ID: 2W6E RELATED DB: PDB
REMARK 900 LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING
REMARK 900 CONTROLLED DEHYDRATION.
REMARK 900 RELATED ID: 2W6F RELATED DB: PDB
REMARK 900 LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING
REMARK 900 CONTROLLED DEHYDRATION: HYDRATION STATE 2.
REMARK 900 RELATED ID: 2W6G RELATED DB: PDB
REMARK 900 LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING
REMARK 900 CONTROLLED DEHYDRATION: HYDRATION STATE 3.
REMARK 900 RELATED ID: 2W6I RELATED DB: PDB
REMARK 900 LOW RESOLUTION STRUCTURES OF BOVINE MITOCHONDRIAL F1-ATPASE DURING
REMARK 900 CONTROLLED DEHYDRATION: HYDRATION STATE 4B.
DBREF 2W6H A -42 510 UNP P19483 ATPA1_BOVIN 1 553
DBREF 2W6H B -42 510 UNP P19483 ATPA1_BOVIN 1 553
DBREF 2W6H C -42 510 UNP P19483 ATPA1_BOVIN 1 553
DBREF 2W6H D -49 478 UNP P00829 ATPB_BOVIN 1 528
DBREF 2W6H E -49 478 UNP P00829 ATPB_BOVIN 1 528
DBREF 2W6H F -49 478 UNP P00829 ATPB_BOVIN 1 528
DBREF 2W6H G -24 273 UNP P05631 ATPG_BOVIN 1 298
DBREF 2W6H H -21 146 UNP P05630 ATPD_BOVIN 1 168
DBREF 2W6H I 0 50 UNP P05632 ATP5E_BOVIN 1 51
SEQRES 1 A 553 MET LEU SER VAL ARG VAL ALA ALA ALA VAL ALA ARG ALA
SEQRES 2 A 553 LEU PRO ARG ARG ALA GLY LEU VAL SER LYS ASN ALA LEU
SEQRES 3 A 553 GLY SER SER PHE ILE ALA ALA ARG ASN LEU HIS ALA SER
SEQRES 4 A 553 ASN SER ARG LEU GLN LYS THR GLY THR ALA GLU VAL SER
SEQRES 5 A 553 SER ILE LEU GLU GLU ARG ILE LEU GLY ALA ASP THR SER
SEQRES 6 A 553 VAL ASP LEU GLU GLU THR GLY ARG VAL LEU SER ILE GLY
SEQRES 7 A 553 ASP GLY ILE ALA ARG VAL HIS GLY LEU ARG ASN VAL GLN
SEQRES 8 A 553 ALA GLU GLU MET VAL GLU PHE SER SER GLY LEU LYS GLY
SEQRES 9 A 553 MET SER LEU ASN LEU GLU PRO ASP ASN VAL GLY VAL VAL
SEQRES 10 A 553 VAL PHE GLY ASN ASP LYS LEU ILE LYS GLU GLY ASP ILE
SEQRES 11 A 553 VAL LYS ARG THR GLY ALA ILE VAL ASP VAL PRO VAL GLY
SEQRES 12 A 553 GLU GLU LEU LEU GLY ARG VAL VAL ASP ALA LEU GLY ASN
SEQRES 13 A 553 ALA ILE ASP GLY LYS GLY PRO ILE GLY SER LYS ALA ARG
SEQRES 14 A 553 ARG ARG VAL GLY LEU LYS ALA PRO GLY ILE ILE PRO ARG
SEQRES 15 A 553 ILE SER VAL ARG GLU PRO MET GLN THR GLY ILE LYS ALA
SEQRES 16 A 553 VAL ASP SER LEU VAL PRO ILE GLY ARG GLY GLN ARG GLU
SEQRES 17 A 553 LEU ILE ILE GLY ASP ARG GLN THR GLY LYS THR SER ILE
SEQRES 18 A 553 ALA ILE ASP THR ILE ILE ASN GLN LYS ARG PHE ASN ASP
SEQRES 19 A 553 GLY THR ASP GLU LYS LYS LYS LEU TYR CYS ILE TYR VAL
SEQRES 20 A 553 ALA ILE GLY GLN LYS ARG SER THR VAL ALA GLN LEU VAL
SEQRES 21 A 553 LYS ARG LEU THR ASP ALA ASP ALA MET LYS TYR THR ILE
SEQRES 22 A 553 VAL VAL SER ALA THR ALA SER ASP ALA ALA PRO LEU GLN
SEQRES 23 A 553 TYR LEU ALA PRO TYR SER GLY CYS SER MET GLY GLU TYR
SEQRES 24 A 553 PHE ARG ASP ASN GLY LYS HIS ALA LEU ILE ILE TYR ASP
SEQRES 25 A 553 ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN MET SER
SEQRES 26 A 553 LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA TYR PRO
SEQRES 27 A 553 GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU ARG
SEQRES 28 A 553 ALA ALA LYS MET ASN ASP ALA PHE GLY GLY GLY SER LEU
SEQRES 29 A 553 THR ALA LEU PRO VAL ILE GLU THR GLN ALA GLY ASP VAL
SEQRES 30 A 553 SER ALA TYR ILE PRO THR ASN VAL ILE SER ILE THR ASP
SEQRES 31 A 553 GLY GLN ILE PHE LEU GLU THR GLU LEU PHE TYR LYS GLY
SEQRES 32 A 553 ILE ARG PRO ALA ILE ASN VAL GLY LEU SER VAL SER ARG
SEQRES 33 A 553 VAL GLY SER ALA ALA GLN THR ARG ALA MET LYS GLN VAL
SEQRES 34 A 553 ALA GLY THR MET LYS LEU GLU LEU ALA GLN TYR ARG GLU
SEQRES 35 A 553 VAL ALA ALA PHE ALA GLN PHE GLY SER ASP LEU ASP ALA
SEQRES 36 A 553 ALA THR GLN GLN LEU LEU SER ARG GLY VAL ARG LEU THR
SEQRES 37 A 553 GLU LEU LEU LYS GLN GLY GLN TYR SER PRO MET ALA ILE
SEQRES 38 A 553 GLU GLU GLN VAL ALA VAL ILE TYR ALA GLY VAL ARG GLY
SEQRES 39 A 553 TYR LEU ASP LYS LEU GLU PRO SER LYS ILE THR LYS PHE
SEQRES 40 A 553 GLU ASN ALA PHE LEU SER HIS VAL ILE SER GLN HIS GLN
SEQRES 41 A 553 ALA LEU LEU SER LYS ILE ARG THR ASP GLY LYS ILE SER
SEQRES 42 A 553 GLU GLU SER ASP ALA LYS LEU LYS GLU ILE VAL THR ASN
SEQRES 43 A 553 PHE LEU ALA GLY PHE GLU ALA
SEQRES 1 B 553 MET LEU SER VAL ARG VAL ALA ALA ALA VAL ALA ARG ALA
SEQRES 2 B 553 LEU PRO ARG ARG ALA GLY LEU VAL SER LYS ASN ALA LEU
SEQRES 3 B 553 GLY SER SER PHE ILE ALA ALA ARG ASN LEU HIS ALA SER
SEQRES 4 B 553 ASN SER ARG LEU GLN LYS THR GLY THR ALA GLU VAL SER
SEQRES 5 B 553 SER ILE LEU GLU GLU ARG ILE LEU GLY ALA ASP THR SER
SEQRES 6 B 553 VAL ASP LEU GLU GLU THR GLY ARG VAL LEU SER ILE GLY
SEQRES 7 B 553 ASP GLY ILE ALA ARG VAL HIS GLY LEU ARG ASN VAL GLN
SEQRES 8 B 553 ALA GLU GLU MET VAL GLU PHE SER SER GLY LEU LYS GLY
SEQRES 9 B 553 MET SER LEU ASN LEU GLU PRO ASP ASN VAL GLY VAL VAL
SEQRES 10 B 553 VAL PHE GLY ASN ASP LYS LEU ILE LYS GLU GLY ASP ILE
SEQRES 11 B 553 VAL LYS ARG THR GLY ALA ILE VAL ASP VAL PRO VAL GLY
SEQRES 12 B 553 GLU GLU LEU LEU GLY ARG VAL VAL ASP ALA LEU GLY ASN
SEQRES 13 B 553 ALA ILE ASP GLY LYS GLY PRO ILE GLY SER LYS ALA ARG
SEQRES 14 B 553 ARG ARG VAL GLY LEU LYS ALA PRO GLY ILE ILE PRO ARG
SEQRES 15 B 553 ILE SER VAL ARG GLU PRO MET GLN THR GLY ILE LYS ALA
SEQRES 16 B 553 VAL ASP SER LEU VAL PRO ILE GLY ARG GLY GLN ARG GLU
SEQRES 17 B 553 LEU ILE ILE GLY ASP ARG GLN THR GLY LYS THR SER ILE
SEQRES 18 B 553 ALA ILE ASP THR ILE ILE ASN GLN LYS ARG PHE ASN ASP
SEQRES 19 B 553 GLY THR ASP GLU LYS LYS LYS LEU TYR CYS ILE TYR VAL
SEQRES 20 B 553 ALA ILE GLY GLN LYS ARG SER THR VAL ALA GLN LEU VAL
SEQRES 21 B 553 LYS ARG LEU THR ASP ALA ASP ALA MET LYS TYR THR ILE
SEQRES 22 B 553 VAL VAL SER ALA THR ALA SER ASP ALA ALA PRO LEU GLN
SEQRES 23 B 553 TYR LEU ALA PRO TYR SER GLY CYS SER MET GLY GLU TYR
SEQRES 24 B 553 PHE ARG ASP ASN GLY LYS HIS ALA LEU ILE ILE TYR ASP
SEQRES 25 B 553 ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN MET SER
SEQRES 26 B 553 LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA TYR PRO
SEQRES 27 B 553 GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU ARG
SEQRES 28 B 553 ALA ALA LYS MET ASN ASP ALA PHE GLY GLY GLY SER LEU
SEQRES 29 B 553 THR ALA LEU PRO VAL ILE GLU THR GLN ALA GLY ASP VAL
SEQRES 30 B 553 SER ALA TYR ILE PRO THR ASN VAL ILE SER ILE THR ASP
SEQRES 31 B 553 GLY GLN ILE PHE LEU GLU THR GLU LEU PHE TYR LYS GLY
SEQRES 32 B 553 ILE ARG PRO ALA ILE ASN VAL GLY LEU SER VAL SER ARG
SEQRES 33 B 553 VAL GLY SER ALA ALA GLN THR ARG ALA MET LYS GLN VAL
SEQRES 34 B 553 ALA GLY THR MET LYS LEU GLU LEU ALA GLN TYR ARG GLU
SEQRES 35 B 553 VAL ALA ALA PHE ALA GLN PHE GLY SER ASP LEU ASP ALA
SEQRES 36 B 553 ALA THR GLN GLN LEU LEU SER ARG GLY VAL ARG LEU THR
SEQRES 37 B 553 GLU LEU LEU LYS GLN GLY GLN TYR SER PRO MET ALA ILE
SEQRES 38 B 553 GLU GLU GLN VAL ALA VAL ILE TYR ALA GLY VAL ARG GLY
SEQRES 39 B 553 TYR LEU ASP LYS LEU GLU PRO SER LYS ILE THR LYS PHE
SEQRES 40 B 553 GLU ASN ALA PHE LEU SER HIS VAL ILE SER GLN HIS GLN
SEQRES 41 B 553 ALA LEU LEU SER LYS ILE ARG THR ASP GLY LYS ILE SER
SEQRES 42 B 553 GLU GLU SER ASP ALA LYS LEU LYS GLU ILE VAL THR ASN
SEQRES 43 B 553 PHE LEU ALA GLY PHE GLU ALA
SEQRES 1 C 553 MET LEU SER VAL ARG VAL ALA ALA ALA VAL ALA ARG ALA
SEQRES 2 C 553 LEU PRO ARG ARG ALA GLY LEU VAL SER LYS ASN ALA LEU
SEQRES 3 C 553 GLY SER SER PHE ILE ALA ALA ARG ASN LEU HIS ALA SER
SEQRES 4 C 553 ASN SER ARG LEU GLN LYS THR GLY THR ALA GLU VAL SER
SEQRES 5 C 553 SER ILE LEU GLU GLU ARG ILE LEU GLY ALA ASP THR SER
SEQRES 6 C 553 VAL ASP LEU GLU GLU THR GLY ARG VAL LEU SER ILE GLY
SEQRES 7 C 553 ASP GLY ILE ALA ARG VAL HIS GLY LEU ARG ASN VAL GLN
SEQRES 8 C 553 ALA GLU GLU MET VAL GLU PHE SER SER GLY LEU LYS GLY
SEQRES 9 C 553 MET SER LEU ASN LEU GLU PRO ASP ASN VAL GLY VAL VAL
SEQRES 10 C 553 VAL PHE GLY ASN ASP LYS LEU ILE LYS GLU GLY ASP ILE
SEQRES 11 C 553 VAL LYS ARG THR GLY ALA ILE VAL ASP VAL PRO VAL GLY
SEQRES 12 C 553 GLU GLU LEU LEU GLY ARG VAL VAL ASP ALA LEU GLY ASN
SEQRES 13 C 553 ALA ILE ASP GLY LYS GLY PRO ILE GLY SER LYS ALA ARG
SEQRES 14 C 553 ARG ARG VAL GLY LEU LYS ALA PRO GLY ILE ILE PRO ARG
SEQRES 15 C 553 ILE SER VAL ARG GLU PRO MET GLN THR GLY ILE LYS ALA
SEQRES 16 C 553 VAL ASP SER LEU VAL PRO ILE GLY ARG GLY GLN ARG GLU
SEQRES 17 C 553 LEU ILE ILE GLY ASP ARG GLN THR GLY LYS THR SER ILE
SEQRES 18 C 553 ALA ILE ASP THR ILE ILE ASN GLN LYS ARG PHE ASN ASP
SEQRES 19 C 553 GLY THR ASP GLU LYS LYS LYS LEU TYR CYS ILE TYR VAL
SEQRES 20 C 553 ALA ILE GLY GLN LYS ARG SER THR VAL ALA GLN LEU VAL
SEQRES 21 C 553 LYS ARG LEU THR ASP ALA ASP ALA MET LYS TYR THR ILE
SEQRES 22 C 553 VAL VAL SER ALA THR ALA SER ASP ALA ALA PRO LEU GLN
SEQRES 23 C 553 TYR LEU ALA PRO TYR SER GLY CYS SER MET GLY GLU TYR
SEQRES 24 C 553 PHE ARG ASP ASN GLY LYS HIS ALA LEU ILE ILE TYR ASP
SEQRES 25 C 553 ASP LEU SER LYS GLN ALA VAL ALA TYR ARG GLN MET SER
SEQRES 26 C 553 LEU LEU LEU ARG ARG PRO PRO GLY ARG GLU ALA TYR PRO
SEQRES 27 C 553 GLY ASP VAL PHE TYR LEU HIS SER ARG LEU LEU GLU ARG
SEQRES 28 C 553 ALA ALA LYS MET ASN ASP ALA PHE GLY GLY GLY SER LEU
SEQRES 29 C 553 THR ALA LEU PRO VAL ILE GLU THR GLN ALA GLY ASP VAL
SEQRES 30 C 553 SER ALA TYR ILE PRO THR ASN VAL ILE SER ILE THR ASP
SEQRES 31 C 553 GLY GLN ILE PHE LEU GLU THR GLU LEU PHE TYR LYS GLY
SEQRES 32 C 553 ILE ARG PRO ALA ILE ASN VAL GLY LEU SER VAL SER ARG
SEQRES 33 C 553 VAL GLY SER ALA ALA GLN THR ARG ALA MET LYS GLN VAL
SEQRES 34 C 553 ALA GLY THR MET LYS LEU GLU LEU ALA GLN TYR ARG GLU
SEQRES 35 C 553 VAL ALA ALA PHE ALA GLN PHE GLY SER ASP LEU ASP ALA
SEQRES 36 C 553 ALA THR GLN GLN LEU LEU SER ARG GLY VAL ARG LEU THR
SEQRES 37 C 553 GLU LEU LEU LYS GLN GLY GLN TYR SER PRO MET ALA ILE
SEQRES 38 C 553 GLU GLU GLN VAL ALA VAL ILE TYR ALA GLY VAL ARG GLY
SEQRES 39 C 553 TYR LEU ASP LYS LEU GLU PRO SER LYS ILE THR LYS PHE
SEQRES 40 C 553 GLU ASN ALA PHE LEU SER HIS VAL ILE SER GLN HIS GLN
SEQRES 41 C 553 ALA LEU LEU SER LYS ILE ARG THR ASP GLY LYS ILE SER
SEQRES 42 C 553 GLU GLU SER ASP ALA LYS LEU LYS GLU ILE VAL THR ASN
SEQRES 43 C 553 PHE LEU ALA GLY PHE GLU ALA
SEQRES 1 D 528 MET LEU GLY LEU VAL GLY ARG VAL VAL ALA ALA SER ALA
SEQRES 2 D 528 SER GLY ALA LEU ARG GLY LEU SER PRO SER ALA PRO LEU
SEQRES 3 D 528 PRO GLN ALA GLN LEU LEU LEU ARG ALA ALA PRO ALA ALA
SEQRES 4 D 528 LEU GLN PRO ALA ARG ASP TYR ALA ALA GLN ALA SER PRO
SEQRES 5 D 528 SER PRO LYS ALA GLY ALA THR THR GLY ARG ILE VAL ALA
SEQRES 6 D 528 VAL ILE GLY ALA VAL VAL ASP VAL GLN PHE ASP GLU GLY
SEQRES 7 D 528 LEU PRO PRO ILE LEU ASN ALA LEU GLU VAL GLN GLY ARG
SEQRES 8 D 528 GLU THR ARG LEU VAL LEU GLU VAL ALA GLN HIS LEU GLY
SEQRES 9 D 528 GLU SER THR VAL ARG THR ILE ALA MET ASP GLY THR GLU
SEQRES 10 D 528 GLY LEU VAL ARG GLY GLN LYS VAL LEU ASP SER GLY ALA
SEQRES 11 D 528 PRO ILE ARG ILE PRO VAL GLY PRO GLU THR LEU GLY ARG
SEQRES 12 D 528 ILE MET ASN VAL ILE GLY GLU PRO ILE ASP GLU ARG GLY
SEQRES 13 D 528 PRO ILE LYS THR LYS GLN PHE ALA ALA ILE HIS ALA GLU
SEQRES 14 D 528 ALA PRO GLU PHE VAL GLU MET SER VAL GLU GLN GLU ILE
SEQRES 15 D 528 LEU VAL THR GLY ILE LYS VAL VAL ASP LEU LEU ALA PRO
SEQRES 16 D 528 TYR ALA LYS GLY GLY LYS ILE GLY LEU PHE GLY GLY ALA
SEQRES 17 D 528 GLY VAL GLY LYS THR VAL LEU ILE MET GLU LEU ILE ASN
SEQRES 18 D 528 ASN VAL ALA LYS ALA HIS GLY GLY TYR SER VAL PHE ALA
SEQRES 19 D 528 GLY VAL GLY GLU ARG THR ARG GLU GLY ASN ASP LEU TYR
SEQRES 20 D 528 HIS GLU MET ILE GLU SER GLY VAL ILE ASN LEU LYS ASP
SEQRES 21 D 528 ALA THR SER LYS VAL ALA LEU VAL TYR GLY GLN MET ASN
SEQRES 22 D 528 GLU PRO PRO GLY ALA ARG ALA ARG VAL ALA LEU THR GLY
SEQRES 23 D 528 LEU THR VAL ALA GLU TYR PHE ARG ASP GLN GLU GLY GLN
SEQRES 24 D 528 ASP VAL LEU LEU PHE ILE ASP ASN ILE PHE ARG PHE THR
SEQRES 25 D 528 GLN ALA GLY SER GLU VAL SER ALA LEU LEU GLY ARG ILE
SEQRES 26 D 528 PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA THR ASP
SEQRES 27 D 528 MET GLY THR MET GLN GLU ARG ILE THR THR THR LYS LYS
SEQRES 28 D 528 GLY SER ILE THR SER VAL GLN ALA ILE TYR VAL PRO ALA
SEQRES 29 D 528 ASP ASP LEU THR ASP PRO ALA PRO ALA THR THR PHE ALA
SEQRES 30 D 528 HIS LEU ASP ALA THR THR VAL LEU SER ARG ALA ILE ALA
SEQRES 31 D 528 GLU LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP SER
SEQRES 32 D 528 THR SER ARG ILE MET ASP PRO ASN ILE VAL GLY SER GLU
SEQRES 33 D 528 HIS TYR ASP VAL ALA ARG GLY VAL GLN LYS ILE LEU GLN
SEQRES 34 D 528 ASP TYR LYS SER LEU GLN ASP ILE ILE ALA ILE LEU GLY
SEQRES 35 D 528 MET ASP GLU LEU SER GLU GLU ASP LYS LEU THR VAL SER
SEQRES 36 D 528 ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO PHE
SEQRES 37 D 528 GLN VAL ALA GLU VAL PHE THR GLY HIS LEU GLY LYS LEU
SEQRES 38 D 528 VAL PRO LEU LYS GLU THR ILE LYS GLY PHE GLN GLN ILE
SEQRES 39 D 528 LEU ALA GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA PHE
SEQRES 40 D 528 TYR MET VAL GLY PRO ILE GLU GLU ALA VAL ALA LYS ALA
SEQRES 41 D 528 ASP LYS LEU ALA GLU GLU HIS SER
SEQRES 1 E 528 MET LEU GLY LEU VAL GLY ARG VAL VAL ALA ALA SER ALA
SEQRES 2 E 528 SER GLY ALA LEU ARG GLY LEU SER PRO SER ALA PRO LEU
SEQRES 3 E 528 PRO GLN ALA GLN LEU LEU LEU ARG ALA ALA PRO ALA ALA
SEQRES 4 E 528 LEU GLN PRO ALA ARG ASP TYR ALA ALA GLN ALA SER PRO
SEQRES 5 E 528 SER PRO LYS ALA GLY ALA THR THR GLY ARG ILE VAL ALA
SEQRES 6 E 528 VAL ILE GLY ALA VAL VAL ASP VAL GLN PHE ASP GLU GLY
SEQRES 7 E 528 LEU PRO PRO ILE LEU ASN ALA LEU GLU VAL GLN GLY ARG
SEQRES 8 E 528 GLU THR ARG LEU VAL LEU GLU VAL ALA GLN HIS LEU GLY
SEQRES 9 E 528 GLU SER THR VAL ARG THR ILE ALA MET ASP GLY THR GLU
SEQRES 10 E 528 GLY LEU VAL ARG GLY GLN LYS VAL LEU ASP SER GLY ALA
SEQRES 11 E 528 PRO ILE ARG ILE PRO VAL GLY PRO GLU THR LEU GLY ARG
SEQRES 12 E 528 ILE MET ASN VAL ILE GLY GLU PRO ILE ASP GLU ARG GLY
SEQRES 13 E 528 PRO ILE LYS THR LYS GLN PHE ALA ALA ILE HIS ALA GLU
SEQRES 14 E 528 ALA PRO GLU PHE VAL GLU MET SER VAL GLU GLN GLU ILE
SEQRES 15 E 528 LEU VAL THR GLY ILE LYS VAL VAL ASP LEU LEU ALA PRO
SEQRES 16 E 528 TYR ALA LYS GLY GLY LYS ILE GLY LEU PHE GLY GLY ALA
SEQRES 17 E 528 GLY VAL GLY LYS THR VAL LEU ILE MET GLU LEU ILE ASN
SEQRES 18 E 528 ASN VAL ALA LYS ALA HIS GLY GLY TYR SER VAL PHE ALA
SEQRES 19 E 528 GLY VAL GLY GLU ARG THR ARG GLU GLY ASN ASP LEU TYR
SEQRES 20 E 528 HIS GLU MET ILE GLU SER GLY VAL ILE ASN LEU LYS ASP
SEQRES 21 E 528 ALA THR SER LYS VAL ALA LEU VAL TYR GLY GLN MET ASN
SEQRES 22 E 528 GLU PRO PRO GLY ALA ARG ALA ARG VAL ALA LEU THR GLY
SEQRES 23 E 528 LEU THR VAL ALA GLU TYR PHE ARG ASP GLN GLU GLY GLN
SEQRES 24 E 528 ASP VAL LEU LEU PHE ILE ASP ASN ILE PHE ARG PHE THR
SEQRES 25 E 528 GLN ALA GLY SER GLU VAL SER ALA LEU LEU GLY ARG ILE
SEQRES 26 E 528 PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA THR ASP
SEQRES 27 E 528 MET GLY THR MET GLN GLU ARG ILE THR THR THR LYS LYS
SEQRES 28 E 528 GLY SER ILE THR SER VAL GLN ALA ILE TYR VAL PRO ALA
SEQRES 29 E 528 ASP ASP LEU THR ASP PRO ALA PRO ALA THR THR PHE ALA
SEQRES 30 E 528 HIS LEU ASP ALA THR THR VAL LEU SER ARG ALA ILE ALA
SEQRES 31 E 528 GLU LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP SER
SEQRES 32 E 528 THR SER ARG ILE MET ASP PRO ASN ILE VAL GLY SER GLU
SEQRES 33 E 528 HIS TYR ASP VAL ALA ARG GLY VAL GLN LYS ILE LEU GLN
SEQRES 34 E 528 ASP TYR LYS SER LEU GLN ASP ILE ILE ALA ILE LEU GLY
SEQRES 35 E 528 MET ASP GLU LEU SER GLU GLU ASP LYS LEU THR VAL SER
SEQRES 36 E 528 ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO PHE
SEQRES 37 E 528 GLN VAL ALA GLU VAL PHE THR GLY HIS LEU GLY LYS LEU
SEQRES 38 E 528 VAL PRO LEU LYS GLU THR ILE LYS GLY PHE GLN GLN ILE
SEQRES 39 E 528 LEU ALA GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA PHE
SEQRES 40 E 528 TYR MET VAL GLY PRO ILE GLU GLU ALA VAL ALA LYS ALA
SEQRES 41 E 528 ASP LYS LEU ALA GLU GLU HIS SER
SEQRES 1 F 528 MET LEU GLY LEU VAL GLY ARG VAL VAL ALA ALA SER ALA
SEQRES 2 F 528 SER GLY ALA LEU ARG GLY LEU SER PRO SER ALA PRO LEU
SEQRES 3 F 528 PRO GLN ALA GLN LEU LEU LEU ARG ALA ALA PRO ALA ALA
SEQRES 4 F 528 LEU GLN PRO ALA ARG ASP TYR ALA ALA GLN ALA SER PRO
SEQRES 5 F 528 SER PRO LYS ALA GLY ALA THR THR GLY ARG ILE VAL ALA
SEQRES 6 F 528 VAL ILE GLY ALA VAL VAL ASP VAL GLN PHE ASP GLU GLY
SEQRES 7 F 528 LEU PRO PRO ILE LEU ASN ALA LEU GLU VAL GLN GLY ARG
SEQRES 8 F 528 GLU THR ARG LEU VAL LEU GLU VAL ALA GLN HIS LEU GLY
SEQRES 9 F 528 GLU SER THR VAL ARG THR ILE ALA MET ASP GLY THR GLU
SEQRES 10 F 528 GLY LEU VAL ARG GLY GLN LYS VAL LEU ASP SER GLY ALA
SEQRES 11 F 528 PRO ILE ARG ILE PRO VAL GLY PRO GLU THR LEU GLY ARG
SEQRES 12 F 528 ILE MET ASN VAL ILE GLY GLU PRO ILE ASP GLU ARG GLY
SEQRES 13 F 528 PRO ILE LYS THR LYS GLN PHE ALA ALA ILE HIS ALA GLU
SEQRES 14 F 528 ALA PRO GLU PHE VAL GLU MET SER VAL GLU GLN GLU ILE
SEQRES 15 F 528 LEU VAL THR GLY ILE LYS VAL VAL ASP LEU LEU ALA PRO
SEQRES 16 F 528 TYR ALA LYS GLY GLY LYS ILE GLY LEU PHE GLY GLY ALA
SEQRES 17 F 528 GLY VAL GLY LYS THR VAL LEU ILE MET GLU LEU ILE ASN
SEQRES 18 F 528 ASN VAL ALA LYS ALA HIS GLY GLY TYR SER VAL PHE ALA
SEQRES 19 F 528 GLY VAL GLY GLU ARG THR ARG GLU GLY ASN ASP LEU TYR
SEQRES 20 F 528 HIS GLU MET ILE GLU SER GLY VAL ILE ASN LEU LYS ASP
SEQRES 21 F 528 ALA THR SER LYS VAL ALA LEU VAL TYR GLY GLN MET ASN
SEQRES 22 F 528 GLU PRO PRO GLY ALA ARG ALA ARG VAL ALA LEU THR GLY
SEQRES 23 F 528 LEU THR VAL ALA GLU TYR PHE ARG ASP GLN GLU GLY GLN
SEQRES 24 F 528 ASP VAL LEU LEU PHE ILE ASP ASN ILE PHE ARG PHE THR
SEQRES 25 F 528 GLN ALA GLY SER GLU VAL SER ALA LEU LEU GLY ARG ILE
SEQRES 26 F 528 PRO SER ALA VAL GLY TYR GLN PRO THR LEU ALA THR ASP
SEQRES 27 F 528 MET GLY THR MET GLN GLU ARG ILE THR THR THR LYS LYS
SEQRES 28 F 528 GLY SER ILE THR SER VAL GLN ALA ILE TYR VAL PRO ALA
SEQRES 29 F 528 ASP ASP LEU THR ASP PRO ALA PRO ALA THR THR PHE ALA
SEQRES 30 F 528 HIS LEU ASP ALA THR THR VAL LEU SER ARG ALA ILE ALA
SEQRES 31 F 528 GLU LEU GLY ILE TYR PRO ALA VAL ASP PRO LEU ASP SER
SEQRES 32 F 528 THR SER ARG ILE MET ASP PRO ASN ILE VAL GLY SER GLU
SEQRES 33 F 528 HIS TYR ASP VAL ALA ARG GLY VAL GLN LYS ILE LEU GLN
SEQRES 34 F 528 ASP TYR LYS SER LEU GLN ASP ILE ILE ALA ILE LEU GLY
SEQRES 35 F 528 MET ASP GLU LEU SER GLU GLU ASP LYS LEU THR VAL SER
SEQRES 36 F 528 ARG ALA ARG LYS ILE GLN ARG PHE LEU SER GLN PRO PHE
SEQRES 37 F 528 GLN VAL ALA GLU VAL PHE THR GLY HIS LEU GLY LYS LEU
SEQRES 38 F 528 VAL PRO LEU LYS GLU THR ILE LYS GLY PHE GLN GLN ILE
SEQRES 39 F 528 LEU ALA GLY GLU TYR ASP HIS LEU PRO GLU GLN ALA PHE
SEQRES 40 F 528 TYR MET VAL GLY PRO ILE GLU GLU ALA VAL ALA LYS ALA
SEQRES 41 F 528 ASP LYS LEU ALA GLU GLU HIS SER
SEQRES 1 G 298 MET PHE SER ARG ALA GLY VAL ALA GLY LEU SER ALA TRP
SEQRES 2 G 298 THR VAL GLN PRO GLN TRP ILE GLN VAL ARG ASN MET ALA
SEQRES 3 G 298 THR LEU LYS ASP ILE THR ARG ARG LEU LYS SER ILE LYS
SEQRES 4 G 298 ASN ILE GLN LYS ILE THR LYS SER MET LYS MET VAL ALA
SEQRES 5 G 298 ALA ALA LYS TYR ALA ARG ALA GLU ARG GLU LEU LYS PRO
SEQRES 6 G 298 ALA ARG VAL TYR GLY VAL GLY SER LEU ALA LEU TYR GLU
SEQRES 7 G 298 LYS ALA ASP ILE LYS THR PRO GLU ASP LYS LYS LYS HIS
SEQRES 8 G 298 LEU ILE ILE GLY VAL SER SER ASP ARG GLY LEU CYS GLY
SEQRES 9 G 298 ALA ILE HIS SER SER VAL ALA LYS GLN MET LYS SER GLU
SEQRES 10 G 298 ALA ALA ASN LEU ALA ALA ALA GLY LYS GLU VAL LYS ILE
SEQRES 11 G 298 ILE GLY VAL GLY ASP LYS ILE ARG SER ILE LEU HIS ARG
SEQRES 12 G 298 THR HIS SER ASP GLN PHE LEU VAL THR PHE LYS GLU VAL
SEQRES 13 G 298 GLY ARG ARG PRO PRO THR PHE GLY ASP ALA SER VAL ILE
SEQRES 14 G 298 ALA LEU GLU LEU LEU ASN SER GLY TYR GLU PHE ASP GLU
SEQRES 15 G 298 GLY SER ILE ILE PHE ASN ARG PHE ARG SER VAL ILE SER
SEQRES 16 G 298 TYR LYS THR GLU GLU LYS PRO ILE PHE SER LEU ASP THR
SEQRES 17 G 298 ILE SER SER ALA GLU SER MET SER ILE TYR ASP ASP ILE
SEQRES 18 G 298 ASP ALA ASP VAL LEU ARG ASN TYR GLN GLU TYR SER LEU
SEQRES 19 G 298 ALA ASN ILE ILE TYR TYR SER LEU LYS GLU SER THR THR
SEQRES 20 G 298 SER GLU GLN SER ALA ARG MET THR ALA MET ASP ASN ALA
SEQRES 21 G 298 SER LYS ASN ALA SER GLU MET ILE ASP LYS LEU THR LEU
SEQRES 22 G 298 THR PHE ASN ARG THR ARG GLN ALA VAL ILE THR LYS GLU
SEQRES 23 G 298 LEU ILE GLU ILE ILE SER GLY ALA ALA ALA LEU ASP
SEQRES 1 H 168 MET LEU PRO SER ALA LEU LEU ARG ARG PRO GLY LEU GLY
SEQRES 2 H 168 ARG LEU VAL ARG GLN VAL ARG LEU TYR ALA GLU ALA ALA
SEQRES 3 H 168 ALA ALA GLN ALA PRO ALA ALA GLY PRO GLY GLN MET SER
SEQRES 4 H 168 PHE THR PHE ALA SER PRO THR GLN VAL PHE PHE ASN SER
SEQRES 5 H 168 ALA ASN VAL ARG GLN VAL ASP VAL PRO THR GLN THR GLY
SEQRES 6 H 168 ALA PHE GLY ILE LEU ALA ALA HIS VAL PRO THR LEU GLN
SEQRES 7 H 168 VAL LEU ARG PRO GLY LEU VAL VAL VAL HIS ALA GLU ASP
SEQRES 8 H 168 GLY THR THR SER LYS TYR PHE VAL SER SER GLY SER VAL
SEQRES 9 H 168 THR VAL ASN ALA ASP SER SER VAL GLN LEU LEU ALA GLU
SEQRES 10 H 168 GLU ALA VAL THR LEU ASP MET LEU ASP LEU GLY ALA ALA
SEQRES 11 H 168 LYS ALA ASN LEU GLU LYS ALA GLN SER GLU LEU LEU GLY
SEQRES 12 H 168 ALA ALA ASP GLU ALA THR ARG ALA GLU ILE GLN ILE ARG
SEQRES 13 H 168 ILE GLU ALA ASN GLU ALA LEU VAL LYS ALA LEU GLU
SEQRES 1 I 51 MET VAL ALA TYR TRP ARG GLN ALA GLY LEU SER TYR ILE
SEQRES 2 I 51 ARG TYR SER GLN ILE CYS ALA LYS ALA VAL ARG ASP ALA
SEQRES 3 I 51 LEU LYS THR GLU PHE LYS ALA ASN ALA MET LYS THR SER
SEQRES 4 I 51 GLY SER THR ILE LYS ILE VAL LYS VAL LYS LYS GLU
HELIX 1 1 ASN A 78 ILE A 82 5 5
HELIX 2 2 GLY A 100 LEU A 104 5 5
HELIX 3 3 ILE A 150 VAL A 157 1 8
HELIX 4 4 GLY A 174 GLN A 186 1 13
HELIX 5 5 GLN A 186 ASP A 191 1 6
HELIX 6 6 LYS A 209 ALA A 223 1 15
HELIX 7 7 ALA A 225 LYS A 227 5 3
HELIX 8 8 ALA A 239 ASN A 260 1 22
HELIX 9 9 ASP A 270 LEU A 285 1 16
HELIX 10 10 GLY A 290 TYR A 294 5 5
HELIX 11 11 ASP A 297 GLU A 307 1 11
HELIX 12 12 ASN A 313 GLY A 317 5 5
HELIX 13 13 ALA A 336 THR A 346 1 11
HELIX 14 14 GLU A 353 LYS A 359 1 7
HELIX 15 15 VAL A 374 GLN A 379 5 6
HELIX 16 16 THR A 380 ALA A 401 1 22
HELIX 17 17 ALA A 402 GLY A 407 5 6
HELIX 18 18 ASP A 411 LEU A 428 1 18
HELIX 19 19 ALA A 437 ARG A 450 1 14
HELIX 20 20 GLU A 457 SER A 459 5 3
HELIX 21 21 LYS A 460 GLN A 475 1 16
HELIX 22 22 HIS A 476 ASP A 486 1 11
HELIX 23 23 SER A 490 GLU A 509 1 20
HELIX 24 24 GLY B 100 LEU B 104 5 5
HELIX 25 25 ILE B 150 VAL B 157 1 8
HELIX 26 26 GLY B 174 GLN B 186 1 13
HELIX 27 27 GLN B 186 ASP B 191 1 6
HELIX 28 28 ASP B 194 LYS B 198 5 5
HELIX 29 29 LYS B 209 ALA B 223 1 15
HELIX 30 30 ALA B 225 LYS B 227 5 3
HELIX 31 31 ALA B 239 ASN B 260 1 22
HELIX 32 32 ASP B 270 LEU B 285 1 16
HELIX 33 33 GLY B 290 TYR B 294 5 5
HELIX 34 34 ASP B 297 ARG B 308 1 12
HELIX 35 35 ASN B 313 GLY B 317 5 5
HELIX 36 36 ALA B 336 SER B 344 1 9
HELIX 37 37 GLU B 353 LYS B 359 1 7
HELIX 38 38 THR B 380 GLU B 399 1 20
HELIX 39 39 ASP B 411 LYS B 429 1 19
HELIX 40 40 ALA B 437 ARG B 450 1 14
HELIX 41 41 GLU B 457 SER B 459 5 3
HELIX 42 42 LYS B 460 GLN B 475 1 16
HELIX 43 43 HIS B 476 GLY B 487 1 12
HELIX 44 44 SER B 490 PHE B 508 1 19
HELIX 45 45 ASN C 78 ILE C 82 5 5
HELIX 46 46 GLY C 100 LEU C 104 5 5
HELIX 47 47 ILE C 150 VAL C 157 1 8
HELIX 48 48 GLY C 174 GLN C 186 1 13
HELIX 49 49 GLN C 186 ASP C 191 1 6
HELIX 50 50 LYS C 209 ALA C 223 1 15
HELIX 51 51 ALA C 225 LYS C 227 5 3
HELIX 52 52 ALA C 239 ASN C 260 1 22
HELIX 53 53 ASP C 270 LEU C 285 1 16
HELIX 54 54 GLY C 290 TYR C 294 5 5
HELIX 55 55 ASP C 297 GLU C 307 1 11
HELIX 56 56 ASN C 313 GLY C 317 5 5
HELIX 57 57 ALA C 336 SER C 344 1 9
HELIX 58 58 GLU C 353 GLY C 360 1 8
HELIX 59 59 VAL C 374 GLN C 379 5 6
HELIX 60 60 THR C 380 GLY C 388 1 9
HELIX 61 61 THR C 389 ALA C 404 1 16
HELIX 62 62 ALA C 412 LEU C 428 1 17
HELIX 63 63 ALA C 437 ARG C 450 1 14
HELIX 64 64 GLU C 457 SER C 459 5 3
HELIX 65 65 LYS C 460 GLN C 475 1 16
HELIX 66 66 HIS C 476 GLY C 487 1 12
HELIX 67 67 SER C 490 GLU C 509 1 20
HELIX 68 68 GLY D 87 THR D 90 5 4
HELIX 69 69 GLU D 122 GLU D 125 5 4
HELIX 70 70 ILE D 137 ALA D 144 1 8
HELIX 71 71 GLY D 161 VAL D 173 1 13
HELIX 72 72 ARG D 189 SER D 203 1 15
HELIX 73 73 PRO D 225 GLN D 246 1 22
HELIX 74 74 ILE D 258 ALA D 270 1 13
HELIX 75 75 LEU D 271 GLY D 273 5 3
HELIX 76 76 SER D 277 TYR D 281 5 5
HELIX 77 77 THR D 284 GLU D 294 1 11
HELIX 78 78 PRO D 313 ASP D 316 5 4
HELIX 79 79 ASP D 319 PHE D 326 1 8
HELIX 80 80 ALA D 327 LEU D 329 5 3
HELIX 81 81 SER D 336 GLU D 341 1 6
HELIX 82 82 ASP D 359 GLY D 364 1 6
HELIX 83 83 GLY D 364 GLY D 392 1 29
HELIX 84 84 SER D 397 LEU D 414 1 18
HELIX 85 85 ALA D 421 GLY D 426 1 6
HELIX 86 86 PRO D 433 ALA D 446 1 14
HELIX 87 87 PRO D 453 TYR D 458 1 6
HELIX 88 88 PRO D 462 ALA D 474 1 13
HELIX 89 89 GLY E 87 LEU E 91 5 5
HELIX 90 90 ILE E 137 ALA E 144 1 8
HELIX 91 91 GLY E 161 GLY E 178 1 18
HELIX 92 92 ARG E 189 SER E 203 1 15
HELIX 93 93 PRO E 225 GLN E 246 1 22
HELIX 94 94 ASN E 257 LEU E 272 1 16
HELIX 95 95 SER E 277 TYR E 281 5 5
HELIX 96 96 THR E 284 GLU E 294 1 11
HELIX 97 97 VAL E 312 ASP E 316 5 5
HELIX 98 98 ASP E 319 ALA E 327 1 9
HELIX 99 99 SER E 336 LEU E 342 1 7
HELIX 100 100 ASP E 359 GLY E 364 1 6
HELIX 101 101 GLY E 364 GLY E 392 1 29
HELIX 102 102 GLU E 399 LEU E 414 1 16
HELIX 103 103 PHE E 418 VAL E 420 5 3
HELIX 104 104 ALA E 421 GLY E 426 1 6
HELIX 105 105 PRO E 433 GLY E 447 1 15
HELIX 106 106 PRO E 453 PHE E 457 5 5
HELIX 107 107 PRO E 462 LEU E 473 1 12
HELIX 108 108 GLY F 87 LEU F 91 5 5
HELIX 109 109 GLU F 122 MET F 126 5 5
HELIX 110 110 ILE F 137 ALA F 144 1 8
HELIX 111 111 GLY F 161 VAL F 173 1 13
HELIX 112 112 ARG F 189 SER F 203 1 15
HELIX 113 113 PRO F 225 GLU F 247 1 23
HELIX 114 114 ILE F 258 ALA F 270 1 13
HELIX 115 115 SER F 277 TYR F 281 5 5
HELIX 116 116 THR F 284 GLU F 294 1 11
HELIX 117 117 PRO F 313 ASP F 316 5 4
HELIX 118 118 ASP F 319 THR F 324 1 6
HELIX 119 119 THR F 325 LEU F 329 5 5
HELIX 120 120 SER F 336 LEU F 342 1 7
HELIX 121 121 ASP F 359 GLY F 392 1 34
HELIX 122 122 SER F 397 LEU F 414 1 18
HELIX 123 123 PHE F 418 VAL F 420 5 3
HELIX 124 124 ALA F 421 GLY F 426 1 6
HELIX 125 125 PRO F 433 ALA F 446 1 14
HELIX 126 126 PRO F 453 TYR F 458 1 6
HELIX 127 127 PRO F 462 ALA F 474 1 13
HELIX 128 128 THR G 2 LEU G 49 1 48
HELIX 129 129 ALA G 80 LEU G 96 1 17
HELIX 130 130 GLY G 109 LEU G 116 1 8
HELIX 131 131 HIS G 117 SER G 121 5 5
HELIX 132 132 THR G 137 ASN G 150 1 14
HELIX 133 133 ALA G 187 ILE G 192 5 6
HELIX 134 134 ASP G 199 LEU G 272 1 74
HELIX 135 135 THR H 99 LEU H 103 5 5
HELIX 136 136 ASP H 104 LEU H 120 1 17
HELIX 137 137 ASP H 124 LYS H 143 1 20
HELIX 138 138 SER I 10 ALA I 25 1 16
SHEET 1 AA14 THR A 28 GLY A 35 0
SHEET 2 AA14 ILE A 87 ARG A 90 -1 O VAL A 88 N GLY A 29
SHEET 3 AA14 MET A 52 PHE A 55 -1 O GLU A 54 N LYS A 89
SHEET 4 AA14 LYS A 60 GLU A 67 -1 O GLY A 61 N VAL A 53
SHEET 5 AA14 THR E 10 ILE E 17 -1 O VAL E 16 N LEU A 66
SHEET 6 AA14 VAL E 20 PHE E 25 -1 O VAL E 20 N ILE E 17
SHEET 7 AA14 THR E 57 ALA E 62 -1 O VAL E 58 N VAL E 23
SHEET 8 AA14 VAL E 46 HIS E 52 -1 O GLU E 48 N ILE E 61
SHEET 9 AA14 ALA E 35 VAL E 38 -1 O LEU E 36 N LEU E 47
SHEET 10 AA14 LYS E 74 ALA E 80 -1 O LEU E 76 N GLU E 37
SHEET 11 AA14 THR E 10 ILE E 17 1 O GLY E 11 N VAL E 75
SHEET 12 AA14 LYS A 60 GLU A 67 -1 O LEU A 66 N VAL E 16
SHEET 13 AA14 MET A 52 PHE A 55 -1 O VAL A 53 N GLY A 61
SHEET 14 AA14 THR A 28 GLY A 35 0
SHEET 1 AB 2 ASP A 96 PRO A 98 0
SHEET 2 AB 2 ARG A 126 ARG A 128 -1 O ARG A 127 N VAL A 97
SHEET 1 AC 8 ARG A 106 VAL A 108 0
SHEET 2 AC 8 THR A 229 ALA A 234 1 O VAL A 231 N VAL A 108
SHEET 3 AC 8 LEU A 199 ILE A 206 1 O CYS A 201 N ILE A 230
SHEET 4 AC 8 HIS A 263 ASP A 269 1 O HIS A 263 N TYR A 200
SHEET 5 AC 8 SER A 320 GLU A 328 1 O SER A 320 N ALA A 264
SHEET 6 AC 8 LEU A 166 GLY A 169 1 O ILE A 167 N ILE A 327
SHEET 7 AC 8 GLY A 348 PHE A 351 1 O GLY A 348 N LEU A 166
SHEET 8 AC 8 VAL A 371 SER A 372 -1 O VAL A 371 N GLN A 349
SHEET 1 AD 2 PRO A 145 MET A 146 0
SHEET 2 AD 2 ILE A 159 GLY A 160 -1 O ILE A 159 N MET A 146
SHEET 1 BA31 THR B 28 GLY B 35 0
SHEET 2 BA31 ILE B 87 ILE B 94 -1 O VAL B 88 N GLY B 29
SHEET 3 BA31 GLU B 51 PHE B 55 -1 O MET B 52 N ALA B 93
SHEET 4 BA31 LYS B 60 GLU B 67 -1 O GLY B 61 N VAL B 53
SHEET 5 BA31 THR F 10 ILE F 17 -1 O VAL F 16 N LEU B 66
SHEET 6 BA31 VAL F 20 PHE F 25 1 O VAL F 20 N ILE F 17
SHEET 7 BA31 THR F 57 ALA F 62 1 O VAL F 58 N VAL F 23
SHEET 8 BA31 VAL F 46 GLY F 54 -1 O GLU F 48 N ILE F 61
SHEET 9 BA31 ALA F 35 VAL F 38 -1 O LEU F 36 N LEU F 47
SHEET 10 BA31 ILE B 38 GLY B 43 0
SHEET 11 BA31 THR B 28 GLY B 35 -1 O ARG B 30 N HIS B 42
SHEET 12 BA31 GLU B 51 PHE B 55 0
SHEET 13 BA31 ILE B 87 ILE B 94 -1 O LYS B 89 N GLU B 54
SHEET 14 BA31 LYS B 60 GLU B 67 0
SHEET 15 BA31 GLU B 51 PHE B 55 -1 O GLU B 51 N SER B 63
SHEET 16 BA31 ASN B 70 VAL B 75 0
SHEET 17 BA31 ILE B 38 GLY B 43 -1 O ALA B 39 N VAL B 73
SHEET 18 BA31 ILE B 87 ILE B 94 0
SHEET 19 BA31 THR B 28 GLY B 35 -1 O GLY B 29 N VAL B 88
SHEET 20 BA31 THR F 10 ILE F 17 0
SHEET 21 BA31 LYS B 60 GLU B 67 -1 O LEU B 66 N VAL F 16
SHEET 22 BA31 VAL F 20 PHE F 25 0
SHEET 23 BA31 THR F 10 ILE F 17 -1 O ARG F 12 N GLN F 24
SHEET 24 BA31 ALA F 35 VAL F 38 0
SHEET 25 BA31 VAL F 46 GLY F 54 -1 O LEU F 47 N LEU F 36
SHEET 26 BA31 VAL F 46 GLY F 54 0
SHEET 27 BA31 ALA F 35 VAL F 38 -1 O LEU F 36 N LEU F 47
SHEET 28 BA31 THR F 57 ALA F 62 0
SHEET 29 BA31 VAL F 20 PHE F 25 1 O VAL F 21 N THR F 60
SHEET 30 BA31 LYS F 74 ASP F 77 0
SHEET 31 BA31 THR F 10 ILE F 17 1 O GLY F 11 N VAL F 75
SHEET 1 BB 2 ASP B 96 VAL B 99 0
SHEET 2 BB 2 ALA B 125 ARG B 128 -1 O ALA B 125 N VAL B 99
SHEET 1 BC11 VAL B 107 VAL B 108 0
SHEET 2 BC11 THR B 229 ALA B 234 1 O VAL B 231 N VAL B 108
SHEET 3 BC11 TYR B 200 ILE B 206 1 O CYS B 201 N ILE B 230
SHEET 4 BC11 HIS B 263 ASP B 269 1 O HIS B 263 N TYR B 200
SHEET 5 BC11 SER B 320 GLU B 328 1 O SER B 320 N ALA B 264
SHEET 6 BC11 ALA B 310 LYS B 311 -1 O ALA B 310 N LEU B 321
SHEET 7 BC11 SER B 320 GLU B 328 -1 O LEU B 321 N ALA B 310
SHEET 8 BC11 VAL B 371 SER B 372 0
SHEET 9 BC11 GLY B 348 PHE B 351 -1 O GLN B 349 N VAL B 371
SHEET 10 BC11 LEU B 166 GLY B 169 1 O LEU B 166 N ILE B 350
SHEET 11 BC11 SER B 320 GLU B 328 1 O PRO B 325 N ILE B 167
SHEET 1 CA12 THR C 28 GLY C 35 0
SHEET 2 CA12 ILE C 87 ILE C 94 -1 O VAL C 88 N GLY C 29
SHEET 3 CA12 ILE C 38 GLY C 43 0
SHEET 4 CA12 THR C 28 GLY C 35 -1 O ARG C 30 N HIS C 42
SHEET 5 CA12 GLU C 51 PHE C 55 0
SHEET 6 CA12 ILE C 87 ILE C 94 -1 O LYS C 89 N GLU C 54
SHEET 7 CA12 LYS C 60 LEU C 66 0
SHEET 8 CA12 GLU C 51 PHE C 55 -1 O GLU C 51 N SER C 63
SHEET 9 CA12 VAL C 71 VAL C 75 0
SHEET 10 CA12 ILE C 38 GLY C 43 -1 O ALA C 39 N VAL C 73
SHEET 11 CA12 ILE C 87 ILE C 94 0
SHEET 12 CA12 THR C 28 GLY C 35 -1 O GLY C 29 N VAL C 88
SHEET 1 CB 2 ASP C 96 VAL C 99 0
SHEET 2 CB 2 ALA C 125 ARG C 128 -1 O ALA C 125 N VAL C 99
SHEET 1 CC 8 VAL C 107 VAL C 108 0
SHEET 2 CC 8 THR C 229 ALA C 234 1 O VAL C 231 N VAL C 108
SHEET 3 CC 8 TYR C 200 ILE C 206 1 O CYS C 201 N ILE C 230
SHEET 4 CC 8 HIS C 263 ASP C 269 1 O HIS C 263 N TYR C 200
SHEET 5 CC 8 SER C 320 GLU C 328 1 O SER C 320 N ALA C 264
SHEET 6 CC 8 LEU C 166 GLY C 169 1 O ILE C 167 N ILE C 327
SHEET 7 CC 8 GLY C 348 LEU C 352 1 O GLY C 348 N LEU C 166
SHEET 8 CC 8 VAL C 371 SER C 372 -1 O VAL C 371 N GLN C 349
SHEET 1 CD 2 PRO C 145 MET C 146 0
SHEET 2 CD 2 ILE C 159 GLY C 160 -1 O ILE C 159 N MET C 146
SHEET 1 DA12 THR D 10 ILE D 17 0
SHEET 2 DA12 LYS D 74 PRO D 81 -1 O VAL D 75 N GLY D 11
SHEET 3 DA12 VAL D 20 PHE D 25 0
SHEET 4 DA12 THR D 10 ILE D 17 -1 O ARG D 12 N GLN D 24
SHEET 5 DA12 ASN D 34 VAL D 38 0
SHEET 6 DA12 LYS D 74 PRO D 81 -1 O LEU D 76 N GLU D 37
SHEET 7 DA12 VAL D 46 HIS D 52 0
SHEET 8 DA12 ASN D 34 VAL D 38 -1 O ASN D 34 N VAL D 49
SHEET 9 DA12 THR D 57 ALA D 62 0
SHEET 10 DA12 VAL D 20 PHE D 25 -1 O VAL D 21 N THR D 60
SHEET 11 DA12 LYS D 74 PRO D 81 0
SHEET 12 DA12 THR D 10 ILE D 17 -1 O GLY D 11 N VAL D 75
SHEET 1 DB 2 ARG D 83 VAL D 86 0
SHEET 2 DB 2 GLN D 112 ALA D 115 -1 O GLN D 112 N VAL D 86
SHEET 1 DC 8 ILE D 94 MET D 95 0
SHEET 2 DC 8 ALA D 216 GLY D 220 1 O LEU D 217 N MET D 95
SHEET 3 DC 8 SER D 181 VAL D 186 1 O SER D 181 N ALA D 216
SHEET 4 DC 8 ASP D 250 ASP D 256 1 O LEU D 252 N VAL D 182
SHEET 5 DC 8 SER D 303 TYR D 311 1 O SER D 303 N VAL D 251
SHEET 6 DC 8 LYS D 151 GLY D 156 1 O ILE D 152 N GLN D 308
SHEET 7 DC 8 ALA D 331 VAL D 334 1 O ALA D 331 N GLY D 153
SHEET 8 DC 8 THR D 354 SER D 355 -1 O THR D 354 N THR D 332
SHEET 1 DD 2 GLU D 131 ILE D 132 0
SHEET 2 DD 2 ALA D 147 LYS D 148 -1 O LYS D 148 N GLU D 131
SHEET 1 EA 2 ARG E 83 VAL E 86 0
SHEET 2 EA 2 GLN E 112 ALA E 115 -1 O GLN E 112 N VAL E 86
SHEET 1 EB 8 ILE E 94 MET E 95 0
SHEET 2 EB 8 VAL E 215 GLN E 221 1 O LEU E 217 N MET E 95
SHEET 3 EB 8 SER E 181 GLU E 188 1 O SER E 181 N ALA E 216
SHEET 4 EB 8 ASP E 250 ASP E 256 1 O LEU E 252 N VAL E 182
SHEET 5 EB 8 SER E 303 ALA E 309 1 O SER E 303 N VAL E 251
SHEET 6 EB 8 LYS E 151 PHE E 155 1 O ILE E 152 N GLN E 308
SHEET 7 EB 8 ALA E 331 VAL E 334 1 O ALA E 331 N GLY E 153
SHEET 8 EB 8 THR E 354 SER E 355 -1 O THR E 354 N THR E 332
SHEET 1 FA 2 ARG F 83 VAL F 86 0
SHEET 2 FA 2 GLN F 112 ALA F 115 -1 O GLN F 112 N VAL F 86
SHEET 1 FB 8 ILE F 94 MET F 95 0
SHEET 2 FB 8 VAL F 215 GLY F 220 1 O LEU F 217 N MET F 95
SHEET 3 FB 8 TYR F 180 VAL F 186 1 O SER F 181 N ALA F 216
SHEET 4 FB 8 ASP F 250 ASP F 256 1 O ASP F 250 N TYR F 180
SHEET 5 FB 8 SER F 303 TYR F 311 1 O SER F 303 N VAL F 251
SHEET 6 FB 8 LYS F 151 GLY F 156 1 O ILE F 152 N GLN F 308
SHEET 7 FB 8 ALA F 331 VAL F 334 1 O ALA F 331 N GLY F 153
SHEET 8 FB 8 THR F 354 SER F 355 -1 O THR F 354 N THR F 332
SHEET 1 FC 2 GLU F 131 LEU F 133 0
SHEET 2 FC 2 TYR F 146 LYS F 148 -1 O TYR F 146 N LEU F 133
SHEET 1 GA 6 SER G 170 ILE G 178 0
SHEET 2 GA 6 GLY G 158 SER G 167 -1 O GLY G 158 N ILE G 178
SHEET 3 GA 6 ILE G 68 VAL G 71 1 O ILE G 69 N ILE G 161
SHEET 4 GA 6 ILE G 105 VAL G 108 1 O ILE G 106 N GLY G 70
SHEET 5 GA 6 VAL G 126 LYS G 129 1 O VAL G 126 N GLY G 107
SHEET 6 GA 6 LYS I 43 VAL I 45 -1 O LYS I 43 N LYS G 129
SHEET 1 HA 5 VAL H 26 VAL H 33 0
SHEET 2 HA 5 MET H 16 ALA H 21 -1 O MET H 16 N VAL H 33
SHEET 3 HA 5 SER H 89 ALA H 94 1 O VAL H 90 N THR H 19
SHEET 4 HA 5 GLY H 80 VAL H 84 -1 O SER H 81 N LEU H 93
SHEET 5 HA 5 THR H 54 VAL H 57 -1 O THR H 54 N VAL H 84
SHEET 1 HB 5 GLY H 46 LEU H 48 0
SHEET 2 HB 5 GLN H 35 ASP H 37 -1 O VAL H 36 N ILE H 47
SHEET 3 HB 5 GLY H 61 HIS H 66 -1 O VAL H 64 N ASP H 37
SHEET 4 HB 5 SER H 73 VAL H 77 -1 O SER H 73 N VAL H 65
SHEET 5 HB 5 ALA H 97 VAL H 98 -1 O VAL H 98 N PHE H 76
CISPEP 1 ASP A 269 ASP A 270 0 -2.21
CISPEP 2 ARG A 362 PRO A 363 0 2.36
CISPEP 3 ASP B 269 ASP B 270 0 -1.48
CISPEP 4 ARG B 362 PRO B 363 0 0.49
CISPEP 5 ASP C 269 ASP C 270 0 -0.93
CISPEP 6 ARG C 362 PRO C 363 0 1.41
CISPEP 7 ASP D 256 ASN D 257 0 5.37
CISPEP 8 TYR D 345 PRO D 346 0 -2.81
CISPEP 9 ASP E 256 ASN E 257 0 -1.07
CISPEP 10 TYR E 345 PRO E 346 0 -1.28
CISPEP 11 ASP F 256 ASN F 257 0 3.57
CISPEP 12 TYR F 345 PRO F 346 0 0.86
CRYST1 107.900 140.240 268.660 90.00 90.00 90.00 P 21 21 21 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009268 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007131 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003722 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
